QOX1_BACSU
ID QOX1_BACSU Reviewed; 649 AA.
AC P34956;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Quinol oxidase subunit 1;
DE EC=1.10.3.-;
DE AltName: Full=Oxidase aa(3)-600 subunit 1;
DE AltName: Full=Quinol oxidase aa3-600, subunit QoxB;
DE AltName: Full=Quinol oxidase polypeptide I;
GN Name=qoxB; OrderedLocusNames=BSU38160; ORFNames=ipa-38d;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=1316894; DOI=10.1016/s0021-9258(19)50007-2;
RA Santana M., Kunst F., Hullo M.-F., Rapoport G., Danchin A., Glaser P.;
RT "Molecular cloning, sequencing, and physiological characterization of the
RT qox operon from Bacillus subtilis encoding the aa3-600 quinol oxidase.";
RL J. Biol. Chem. 267:10225-10231(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=7934828; DOI=10.1111/j.1365-2958.1993.tb01963.x;
RA Glaser P., Kunst F., Arnaud M., Coudart M.P., Gonzales W., Hullo M.-F.,
RA Ionescu M., Lubochinsky B., Marcelino L., Moszer I., Presecan E.,
RA Santana M., Schneider E., Schweizer J., Vertes A., Rapoport G., Danchin A.;
RT "Bacillus subtilis genome project: cloning and sequencing of the 97 kb
RT region from 325 degrees to 333 degrees.";
RL Mol. Microbiol. 10:371-384(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
CC -!- FUNCTION: Catalyzes quinol oxidation with the concomitant reduction of
CC oxygen to water. Major component for energy conversion during
CC vegetative growth (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 a quinol + O2 = 2 a quinone + 2 H2O; Xref=Rhea:RHEA:55376,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:24646,
CC ChEBI:CHEBI:132124;
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250};
CC Note=Binds a copper B center. {ECO:0000250};
CC -!- COFACTOR:
CC Name=ferriheme a; Xref=ChEBI:CHEBI:60532; Evidence={ECO:0000250};
CC -!- COFACTOR:
CC Note=Heme A3. {ECO:0000250};
CC -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the heme-copper respiratory oxidase family.
CC {ECO:0000305}.
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DR EMBL; M86548; AAA22687.1; -; Genomic_DNA.
DR EMBL; X73124; CAA51594.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15842.1; -; Genomic_DNA.
DR PIR; B38129; B38129.
DR RefSeq; NP_391695.1; NC_000964.3.
DR RefSeq; WP_003227407.1; NZ_JNCM01000034.1.
DR PDB; 6KOB; X-ray; 3.60 A; A/E=1-649.
DR PDB; 6KOC; X-ray; 3.80 A; A/E=1-649.
DR PDB; 6KOE; X-ray; 3.75 A; A/E=1-649.
DR PDBsum; 6KOB; -.
DR PDBsum; 6KOC; -.
DR PDBsum; 6KOE; -.
DR AlphaFoldDB; P34956; -.
DR SMR; P34956; -.
DR STRING; 224308.BSU38160; -.
DR PaxDb; P34956; -.
DR PRIDE; P34956; -.
DR EnsemblBacteria; CAB15842; CAB15842; BSU_38160.
DR GeneID; 937303; -.
DR KEGG; bsu:BSU38160; -.
DR PATRIC; fig|224308.179.peg.4130; -.
DR eggNOG; COG0843; Bacteria.
DR InParanoid; P34956; -.
DR OMA; WAMMSIG; -.
DR PhylomeDB; P34956; -.
DR BioCyc; BSUB:BSU38160-MON; -.
DR BioCyc; MetaCyc:BSU38160-MON; -.
DR UniPathway; UPA00705; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0016682; F:oxidoreductase activity, acting on diphenols and related substances as donors, oxygen as acceptor; ISS:UniProtKB.
DR GO; GO:0009060; P:aerobic respiration; IBA:GO_Central.
DR GO; GO:0042773; P:ATP synthesis coupled electron transport; ISS:UniProtKB.
DR GO; GO:0015990; P:electron transport coupled proton transport; IBA:GO_Central.
DR GO; GO:0022904; P:respiratory electron transport chain; IBA:GO_Central.
DR Gene3D; 1.20.210.10; -; 1.
DR InterPro; IPR023616; Cyt_c_oxase-like_su1_dom.
DR InterPro; IPR036927; Cyt_c_oxase-like_su1_sf.
DR InterPro; IPR000883; Cyt_C_Oxase_1.
DR InterPro; IPR023615; Cyt_c_Oxase_su1_BS.
DR InterPro; IPR014233; QoxB.
DR PANTHER; PTHR10422; PTHR10422; 1.
DR Pfam; PF00115; COX1; 1.
DR PRINTS; PR01165; CYCOXIDASEI.
DR SUPFAM; SSF81442; SSF81442; 1.
DR TIGRFAMs; TIGR02882; QoxB; 1.
DR PROSITE; PS50855; COX1; 1.
DR PROSITE; PS00077; COX1_CUB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Copper; Electron transport; Heme;
KW Hydrogen ion transport; Ion transport; Iron; Membrane; Metal-binding;
KW Oxidoreductase; Reference proteome; Respiratory chain; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..649
FT /note="Quinol oxidase subunit 1"
FT /id="PRO_0000183474"
FT TOPO_DOM 1..15
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 16..34
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 35..56
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 57..75
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 76..97
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 98..117
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 118..139
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 140..157
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 158..190
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 191..209
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 210..227
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 228..246
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 247..272
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 273..292
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 293..315
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 316..335
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 336..343
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 344..362
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 363..377
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 378..397
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 398..405
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 406..425
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 426..452
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 453..472
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 473..490
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 491..510
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 511..584
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 585..604
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 605..610
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 611..631
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 632..649
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT BINDING 102
FT /ligand="Fe(II)-heme a"
FT /ligand_id="ChEBI:CHEBI:61715"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT BINDING 280
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250"
FT BINDING 284
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250"
FT BINDING 329
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250"
FT BINDING 330
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250"
FT BINDING 415
FT /ligand="heme a3"
FT /ligand_id="ChEBI:CHEBI:83282"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT BINDING 417
FT /ligand="Fe(II)-heme a"
FT /ligand_id="ChEBI:CHEBI:61715"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT CROSSLNK 280..284
FT /note="1'-histidyl-3'-tyrosine (His-Tyr)"
FT /evidence="ECO:0000250"
SQ SEQUENCE 649 AA; 73838 MW; 5D77F58ED64CBFCC CRC64;
MKFKWDEFFV TGDPLILGAQ VSIALSTIAI IFVLTYFKKW KWLWSEWITT VDHKKLGIMY
IISAVIMLFR GGVDGLMMRA QLALPNNSFL DSNHYNEIFT THGTIMIIFM AMPFLIGLIN
VVVPLQIGAR DVAFPYLNNL SFWTFFVGAM LFNISFVIGG SPNAGWTSYM PLASNDMSPG
PGENYYLLGL QIAGIGTLMT GINFMVTILK MRTKGMTLMR MPMFTWTTLI TMVIIVFAFP
VLTVALALLS FDRLFGAHFF TLEAGGMPML WANLFWIWGH PEVYIVILPA FGIFSEIISS
FARKQLFGYK AMVGSIIAIS VLSFLVWTHH FFTMGNSASV NSFFSITTMA ISIPTGVKIF
NWLFTMYKGR ISFTTPMLWA LAFIPNFVIG GVTGVMLAMA AADYQYHNTY FLVSHFHYVL
IAGTVFACFA GFIFWYPKMF GHKLNERIGK WFFWIFMIGF NICFFPQYFL GLQGMPRRIY
TYGPNDGWTT LNFISTVGAF MMGVGFLILC YNIYYSFRYS TREISGDSWG VGRTLDWATS
SAIPPHYNFA VLPEVKSQDA FLHMKEEKTE LYPESKFKKI HMPSNSGRPF FMSVAFGLAG
FGLVFEWYWM GVVGLIGVLL CMVLRSFEYD NGYYISVDEI KETERKISE
